| pubmed-article:14726530 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C0013878 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C1158923 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C0728938 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:14726530 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:14726530 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:14726530 | pubmed:dateCreated | 2004-3-29 | lld:pubmed |
| pubmed-article:14726530 | pubmed:abstractText | We developed a novel and generalized approach to investigate G protein-coupled receptor molecular assemblies. We solubilized a fusion protein consisting of the beta(2)-adrenergic receptor and green fluorescent protein (GFP) for bead-based flow cytometric analysis. beta(2)-Adrenergic receptor GFP bound to dihydroalprenolol-conjugated beads, providing a K(d) for the fusion protein and, in competition with beta(2)-adrenergic receptor ligands, K(d) values for agonists and antagonists. Beads displaying chelated nickel bound purified hexahistidine-tagged G protein heterotrimers and, subsequently, the binary complex of agonist with beta(2)-adrenergic receptor GFP. The dose-response curves of ternary complex formation revealed maximal assembly for ligands previously classified as full agonists and reduced assembly for ligands previously classified as partial agonists. Guanosine 5'-3-O-(thio)triphosphate-induced dissociation rates of the ternary complex were the same for full and partial agonists. Soluble G protein, competing with ternary complexes on beads provided an affinity estimate of agonist-receptor complexes to G protein. When performed simultaneously, the two assemblies discriminated between agonist, antagonist or inactive molecule in a manner appropriate for high throughput, small volume drug discovery. The assemblies can be further generalized to other G protein coupled receptor protein-protein interactions. | lld:pubmed |
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| pubmed-article:14726530 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14726530 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14726530 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14726530 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14726530 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14726530 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14726530 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:14726530 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:TangWei-JenWJ | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:SklarLarry... | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:ProssnitzEric... | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:NeubigRichard... | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:GuoQingQ | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:CiminoDaniel... | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:SimonsPeter... | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:FoutzTerryT | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:WallerAnnaA | lld:pubmed |
| pubmed-article:14726530 | pubmed:author | pubmed-author:BiggsSean MSM | lld:pubmed |
| pubmed-article:14726530 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14726530 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:14726530 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:14726530 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14726530 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14726530 | pubmed:pagination | 13514-21 | lld:pubmed |
| pubmed-article:14726530 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:14726530 | pubmed:meshHeading | pubmed-meshheading:14726530... | lld:pubmed |
| pubmed-article:14726530 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14726530 | pubmed:articleTitle | Real-time analysis of ternary complex on particles: direct evidence for partial agonism at the agonist-receptor-G protein complex assembly step of signal transduction. | lld:pubmed |
| pubmed-article:14726530 | pubmed:affiliation | Department of Pathology, University of New Mexico Health Sciences Center, Albuquerque, New Mexico 87131, USA. | lld:pubmed |
| pubmed-article:14726530 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14726530 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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